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1.
Indian J Exp Biol ; 2004 Jan; 42(1): 86-90
Article in English | IMSEAR | ID: sea-58679

ABSTRACT

In the present study tentative link has been established between H+ -efflux and effect of NO in presence of various nutrients (glucose, 2-deoxy-D-glucose, xylose, proline, glutamic acid and lysine) in C. albicans using sodium nitroprusside (SNP) as a potent source of NO. It was observed that there was a decreasing trend in pH with time, in control, while SNP treated cells showed an initial decline in pH for 10-15 min, followed by an increase in pH up to 30 min. In presence of glucose there was an enhancement in H+ -efflux by 9-fold whereas proline, glutamic acid and lysine showed enhancement by 3, 6 and 1.5-fold respectively. Similar trends in increase in pH after 15 min in SNP treated cells of Candida was observed in presence of all nutrients used. It was demonstrated for the first time that H+ -ATPase of C. albicans was affected by NO.


Subject(s)
Adenosine Triphosphatases/metabolism , Adenosine Triphosphate/metabolism , Biological Transport , Candida albicans/drug effects , Hydrogen-Ion Concentration , Ions , Nitric Oxide/metabolism , Nitroprusside/metabolism , Proton-Translocating ATPases/chemistry , Protons , Time Factors
3.
Indian J Biochem Biophys ; 2001 Jun; 38(3): 149-52
Article in English | IMSEAR | ID: sea-28583

ABSTRACT

High resolution [31P] nuclear magnetic resonance (NMR) spectroscopy was used to investigate the changes in phosphate metabolism and intracellular pH in intact root segments of relatively osmotic stress sensitive species maize (Zea mays L) and insensitive species pearl millet (Pennisetron americanum (L) Leeke) exposed to hyper osmotic shock. The results were used to understand the adaptive mechanism of the two species. The hyper osmotic shock resulted in large build-up of phosphocholine and decrease in glucose 6-phosphate (G-6P) and UDPG levels in both the crops. The osmotic shock produced a large vacuolar alkalinization and decrease in pH across tonoplast membrane in maize roots. However, the roots of pearl millet were able to adapt to the stress and maintained pH gradient across tonoplast with marginal vacuolar alkalinization. This may be attributed to the sustained activity of primary tonoplast pumps and increased activity of H+-ATPase that normally maintain pH gradient across tonoplast.


Subject(s)
Cell Membrane/enzymology , Hydrogen-Ion Concentration , Magnetic Resonance Spectroscopy , Osmotic Pressure , Panicum/enzymology , Proton-Translocating ATPases/chemistry , Time Factors , Zea mays/genetics
4.
Indian J Biochem Biophys ; 2001 Jun; 38(3): 199-202
Article in English | IMSEAR | ID: sea-28255

ABSTRACT

H+-ATPase activity in leaves and roots of coconut palms growing in 'root wilt disease-prevalent areas' was compared with that of coconut palms growing in 'disease-free areas'. The activity was found to be significantly less in the leaves and roots of palms in the disease-prevalent zone as compared to that in disease-free zone. Histochemical examination of the leaves showed results that corroborated the biochemical findings. The possible application of H+-ATPase activity as a marker for the early detection of wilt disease in coconut palms is suggested.


Subject(s)
Cocos/chemistry , Microscopy, Electron, Scanning , Plant Diseases , Plant Leaves/enzymology , Proton-Translocating ATPases/chemistry
5.
Biol. Res ; 29(1): 31-46, 1996.
Article in English | LILACS | ID: lil-228547

ABSTRACT

Photoaffinity labeling is a special type of chemical modification, where the label is activated by the action of light. This article presents the general principles and limitations of this technique, its application to the study of Micrococcus luteus ATPase and the use of photoaffinity crosslinking to probe the structure of this enzyme


Subject(s)
Adenosine Diphosphate/chemistry , Adenosine Triphosphate/chemistry , Affinity Labels/chemistry , Enzyme Activation/physiology , Free Radicals/chemistry , Ligands , Micrococcus luteus/enzymology , Peptides/chemistry , Protein Conformation , Proton-Translocating ATPases/chemistry , Proton-Translocating ATPases/ultrastructure
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